大鼠与家兔生后各年龄阶段跖肌纤维的比较

应用建立在肌球蛋白重链异构体基础上的标准肌动球蛋白ATP酶和琥珀酸脱氢酶组织化学方法,分析大鼠和家兔出生后发育各年龄阶段跖肌纤维型分布。在生后2周至24周龄的大鼠和家兔Ⅰ、ⅡX型肌纤维百分比例减少,而ⅡA、ⅡB型纤维则增加。进行大量单肌纤维的组织化学特征的比较和相关性探讨。结果显示动物平均体重与跖肌的平均湿重随生后发育逐渐增加,Ⅰ、ⅡX、ⅡA及ⅡB型纤维均在生后各年龄组的全部肌肉内被发现,但出生后2日龄组是个例外。在生后发育期间,雄性大鼠和家兔ⅡB型纤维的平均肌纤维型构成要大于雌性大鼠和家兔,而雄性大鼠和家兔Ⅰ、ⅡX、ⅡA型三种氧化组织化学分类的肌纤维型构成均小于雌性大鼠和家兔。大鼠Ⅰ、ⅡX、ⅡA和ⅡB型纤维的平均横切面积显然要比家兔的同类型肌纤维要小。在大鼠和家兔可见明显的性别差异。大鼠和家兔的ⅡX型纤维横切面积是最小的,Ⅰ、ⅡA型纤维呈中等大小,ⅡB型纤维最大。该重要的测试有助于我们深入研究啮齿类动物快肌纤维生理特征的适应。     

Evidence for three fast myosin heavy chain isoforms in type II skeletal muscle fibers in the adult llama (Lama glama).

Skeletal muscle fiber types classified on the basis of their content of different myosin heavy chain (MHC) isoforms were analyzed in samples from hindlimb muscles of adult sedentary llamas (Lama glama) by correlating immunohistochemistry with specific anti-MHC monoclonal antibodies, myofibrillar ATPase (mATPase) histochemistry, and quantitative histochemistry of fiber metabolic and size properties. The immunohistochemical technique allowed the separation of four pure (i.e., expressing a unique MHC isoform) muscle fiber types: one slow-twitch (Type I) and three fast-twitch (Type II) phenotypes. The same four major fiber types could be objectively discriminated with two serial sections stained for mATPase after acid (pH 4.5) and alkaline (pH 10.5) preincubations. The three fast-twitch fiber types were tentatively designated as IIA, IIX, and IIB on the basis of the homologies of their immunoreactivities, acid denaturation of their mATPase activity, size, and metabolic properties expressed at the cellular level with the corresponding isoforms of rat and horse muscles. Acid stability of their mATPase activity increased in the rank order IIA>IIX>IIB. The same was true for size and glycolytic capacity, whereas oxidative capacity decreased in the same rank order IIA>IIX>IIB. In addition to these four pure fibers (I, IIA, IIX, and IIB), four other fiber types with hybrid phenotypes containing two (I+IIA, IIAX, and IIXB) or three (IIAXB) MHCs were immunohistochemically delineated. These frequent phenotypes (40% of the semitendinosus muscle fiber composition) had overlapped mATPase staining intensities with their corresponding pure fiber types, so they could not be delineated by mATPase histochemistry. Expression of the three fast adult MHC isoforms was spatially regulated around islets of Type I fibers, with concentric circles of fibers expressing MHC-IIA, then MHC-IIX, and peripherally MHC-IIB. This study demonstrates that three adult fast Type II MHC isoproteins are expressed in skeletal muscle fibers of the llama. The general assumption that the very fast MHC-IIB isoform is expressed only in small mammals can be rejected.     

Fiber composition and oxidative capacity of hamster skeletal muscle.

The hamster is a valuable biological model for physiological investigation. Despite the obvious importance of the integration of cardiorespiratory and muscular system function, little information is available regarding hamster muscle fiber type and oxidative capacity, both of which are key determinants of muscle function. The purpose of this investigation was to measure immunohistochemically the relative composition and size of muscle fibers composed of types I, IIA, IIX, and IIB fibers in hamster skeletal muscle. The oxidative capacity of each muscle was also assessed by measuring citrate synthase activity. Twenty-eight hindlimb, respiratory, and facial muscles or muscle parts from adult (144-147 g bw) male Syrian golden hamsters (n=3) were dissected bilaterally, weighed, and frozen for immunohistochemical and biochemical analysis. Combining data from all 28 muscles analyzed, type I fibers made up 5% of the muscle mass, type IIA fibers 16%, type IIX fibers 39%, and type IIB fibers 40%. Mean fiber cross-sectional area across muscles was 1665 +/- 328 microm(2) for type I fibers, 1900 +/- 417 microm(2) for type IIA fibers, 3230 +/- 784 microm(2) for type IIX fibers, and 4171 +/- 864 microm(2) for type IIB fibers. Citrate synthase activity was most closely related to the population of type IIA fibers (r=0.68, p<0.0001) and was in the rank order of type IIA > I > IIX > IIB. These data demonstrate that hamster skeletal muscle is predominantly composed of type IIB and IIX fibers.     

Fiber type composition of the vastus lateralis muscle of young men and women.

This study presents data collected over the past 10 years on the muscle fiber type composition of the vastus lateralis muscle of young men and women. Biopsies were taken from the vastus lateralis muscle of 55 women (21.2+/-2.2 yr) and 95 men (21.5+/-2.4 yr) who had volunteered to participate in various research projects. Six fiber types (I, IC, IIC, IIA, IIAB, and IIB) were classified using mATPase histochemistry, and cross-sectional area was measured for the major fiber types (I, IIA, and IIB). Myosin heavy chain (MHC) content was determined electrophoretically on all of the samples from the men and on 26 samples from the women. With the exception of fiber Type IC, no significant differences were found between men and women for muscle fiber type distribution. The vastus lateralis muscle of both the men and women contained approximately 41% I, 1% IC, 1% IIC, 31% IIA, 6% IIAB, and 20% IIB. However, the cross-sectional area of all three major fiber types was larger for the men compared to the women. In addition, the Type IIA fibers were the largest for the men, whereas the Type I fibers tended to be the largest for the women. Therefore, gender differences were found with regard to the area occupied by each specific fiber type: IIA>I>IIB for the men and I>IIA>IIB for the women. These data establish normative values for the mATPase-based fiber type distribution and sizes in untrained young men and women.     

Direct correlation of parvalbumin levels with myosin isoforms and succinate dehydrogenase activity on frozen sections of rodent muscle

Parvalbumin (PV) is a soluble Ca++ binding protein which is particularly concentrated in fast muscles of rodents. We have developed a new protocol to fix frozen sections of muscle by formaldehyde vapor, which enabled us to immunochemically stain serial frozen sections for PV. Fiber types were defined on the basis of myosin ATPase stability, and of isomyosins identified by a variety of antibodies because ATPase stability alone yielded ambiguous results in the mouse. Slow Type I fibers in mouse and rat were devoid of PV and had intermediate to high SDH levels. Fast fiber subtypes IIA, IIB, and IIX-like were defined in the mouse on the basis of the similarity of their myosin heavy chain immunoreactivity to these types in the rat. The soleus muscle was usually PV negative, but a small population of strongly PV-positive IIX-like fibers was present in the mouse. In mouse fast muscle, small diameter IIA fibers were PV negative with high SDH activity. In both mouse and rat, PV reactivities of IIB and IIX fibers were higher than those of IIA and I, whereas SDH levels of IIA, IIX, and I fibers were higher than those of IIB. Thus, PV content correlated with the type of myosin ATPase but not with SDH levels. The method described for immunocytochemistry of PV may be applicable to other highly soluble proteins.     

Fiber type population in limb muscles ofMicrocebus murinus

Populations and distributions of fiber types were studied in 19 limb muscles ofMicrocebus murinus. Proportions and cross-sectional areas of muscles fiber types were compared with data from the literature for other prosimians (Galago, Lemur, andNycticebus), another primate (Macaca cynomolgus), and the rat. Most muscles are heterogenous, with type I fibers (slow oxidative) localized in the deeper part, near the bone. Type IIA fibers (fast oxidative glycolytic) are more evenly distributed than type I and type IIB (fast glycolytic). The combination of large number and large size of type I fibers results in enhanced slow-twitch and oxidative properties as required for antigravity function of postural muscles. Compared with other primates,Microcebus shows relatively small cross-sectional areas of fibers and less numerous type I fibers, in every muscle, which is probably related to small body mass. The fiber type population of the different components of the quadriceps femoris is also related to the particular mode of locomotion of the mouse-lemur: running and leaping, climbing and hopping. M. vastus medialis and m. vastus lateralis are made up only of fast twitch fibers, IIA and IIB. A possible repercussion of hypothyroidism during the rest season and a decrease in locomotor activity was the subject of investigation of the fiber type proportion and section areas. No difference were found between individuals euthanized during the active period and those at rest period. Either a very low level of thyroxine associated with reduced activity is sufficient to maintain the processes controlling myosin expression, or the effects on muscles fibers of natural hypothyroidism and hypokinesia neutralize each other during the rest season.     

Purification and characterization of myosins from human and rabbit skeletal muscles by using specific monoclonal antibodies

By using immunoaffinity column chromatography slow (I) and fast (IIA, IIB) myosins were isolated from human (vastus lateralis) and rabbit (tibialis anterior, psoas and conoidal bundle) skeletal muscles. The peptide pattern revealed that slow (I) and fast (IIA, IIB) myosin heavy chains are quite distinct, as are those from pure slow (conoidal bundle) and fast (psoas) rabbit skeletal muscles. Unlike Billeter et al. (1981) the authors observed that fast human myosins were always associated with a small amount of slow myosin light chains. The fast myosins (IIA, IIB) from rabbit tibialis anterior muscle did not appear very distinct and contained only fast myosin light chains. These myosins were different from the IIB myosin from the psoas muscle. Ten per cent of the fibres revealed histochemically as fast IIA also reacted with an anti-slow myosin antibody. The classical histochemical techniques appear inadequate to demonstrate the existing differences among fibre types, but the monoclonal antibodies hold promise.     

Misclassification of hybrid fast fibers in resistance-trained human skeletal muscle using histochemical and immunohistochemical methods

ABSTRACT: Staron, RS, Herman, JR, and Schuenke, MD. Misclassification of hybrid fast fibers in resistance-trained human skeletal muscle using histochemical and immunohistochemical methods. J Strength Cond Res 26(10): 2616-2622, 2012-Sixteen healthy untrained women participated in a 6-week progressive resistance training program to compare 2 common methods of classifying fiber types. The women were a subset from a previous study and were randomly divided into 2 groups: traditional strength training (TS, n = 9) and non-exercising control (C, n = 7). The TS group performed 3 lower limb exercises (leg press, squat, and knee extension) using 6-10 repetitions maximum 2 days per week for the first week and 3 days per week for the remaining 5 weeks (17 total workouts). Pre- and posttraining vastus lateralis muscle biopsies were analyzed for fiber type composition using 2 popular methods: myosin adenosine triphosphatase (mATPase) histochemistry and myosin heavy chain (MHC) immunohistochemistry. Six fiber types (I, IC, IIC, IIA, IIAX, and IIX) were delineated using each method separately and in combination. Because of the subjective nature of each method (visual assessment of staining intensities), IIAX fibers expressing a small amount of MHCIIa were misclassified as type IIX using mATPase histochemistry, whereas those expressing a small amount of MHCIIx were misclassified as type IIA using MHC immunohistochemistry. As such, either method used separately resulted in an underestimation of the type IIAX fiber population. In addition, the use of mATPase histochemistry alone resulted in an overestimation of type IIX, whereas there was an overestimation of type IIA using MHC immunohistochemistry. These fiber typing errors were most evident after 6 weeks of resistance training when fibers were in transition from type IIX to IIA. These data suggest that the best approach to more accurately determine muscle fiber type composition (especially after training) is the combination of mATPase histochemical and MHC immunohistochemical methods.     

Mouse transgenic lines that selectively label Type I, Type IIA, and Types IIX+B skeletal muscle fibers

Skeletal muscle fibers vary in contractile and metabolic properties. Four main fiber types are present in mammalian trunk and limb muscles; they are called I, IIA, IIX, and IIB, ranging from slowest- to fastest-contracting. Individual muscles contain stereotyped proportions of two or more fiber types. Fiber type is determined by a combination of nerve-dependent and -independent influences, leading to formation of "homogeneous motor units" in which all branches of a single motor neuron form synapses on fibers of a single type. Fiber type composition of muscles can be altered in adulthood by multiple factors including exercise, denervation, hormones, and aging. To facilitate analysis of muscle development, plasticity, and innervation, we generated transgenic mouse lines in which Type I, Type IIA, and Type IIX+B fibers can be selectively labeled with distinguishable fluorophores. We demonstrate their use for motor unit reconstruction and live imaging of nerve-dependent alterations in fiber type.     

Muscle fiber characteristics and performance correlates of male Olympic-style weightlifters

Biopsies fro the vastus lateralis muscle of male weightlifters (WL; n=6; X +/- SE, age=27.0 +/- 2.1 years), and non-weight-trained men (CON; n=7; age=27.0 +/- 2.0 years) were compared for fiber types, myosin heavy chain (MHC) and titin content, and fiber type-specific capillary density. Differences (p<0.05) were observed for percent fiber types IIC (WL=0.4 +/- 0.2, CON=2.4 +/- 0.8); IIA (WL=50.5 +/- 3.2, CON=26.9 +/- 3.7); and IIB (WL=1.7 +/- 1.4, CON=21.0 +/- 5.3), as well as percent MHC IIa (WL=65.3 +/- 2.4, CON=52.1 +/- 4.2) and percent MHC IIB (WL=0.9 +/- 0.9; CON=18.2 +/- 6.1). All WL exhibited only the titin-1 isoform. Capillary density (caps.mm(-2)) for all fiber types combined was greater for the CON subjects (WL=192.7 +/- 17.3; CON=262.9 +/- 26.3), due primarily to a greater capillary density in the IIA fibers. Weightlifting performances and vertical jump power were correlated with type II fiber characteristics. These results suggest that successful weightlifting performance is not dependent on IIB fibers, and that weightlifters exhibit large percentages of type IIA muscle fibers and MHC IIa isoform content.     

Specific isomyosin proportions in hyperexcitable and physiologically denervated mouse muscle

We show here, by high resolution sodium dodecyl sulfate gel electrophoresis, that the proportions of myosin heavy chain (MyHC) isoforms of mouse muscles are specifically shifted by hereditary neuromuscular diseases. In wild-type and dystrophic MDX anterior tibial muscle (TA) about 60% of the MyHC is IIB, 30% IIX, at most 10% IIA and <2% type I (slow). In myotonic fast muscles, hyperexcitability leads to a drastic reduction of MyHC IIB which is compensated by IIA. Slow muscles, like soleus and diaphragm, were only marginally changed by myotonia. The MyHC pattern of TA of spinal muscular atrophy (SMA) 'wobbler' mice is shifted to a faster phenotype, with nearly 90% IIB. In the SMA mutant 'muscle deficient', all four adult isomyosins are expressed in the TA. These findings may be relevant for the future diagnosis of neurological disorders both in mouse disease models and in human patients.     

Postmortem alterations in the pH range of myofibrillar ATPase activation/inactivation

A histochemical assay for myofibrillar adenosine triphosphatase (mATPase) activity is routinely utilized in the delineation of fiber types in healthy human skeletal muscle. Each fiber type has a specific pH range of mATPase stability (activation). Outside of this pH range, mATPase activity is labile (inactivated), no reaction product is formed, and the fibers remain unstained. The aim of the present study was to carefully investigate the pH stability/lability of mATPase in postmortem muscles. To this end, vastus lateralis muscle samples were obtained approximately 0.5, 1, 2, 3, and 4 days after death, as well as control samples from a healthy young man and woman. Serial cross sections of the muscle samples were assayed for mATPase activity throughout preincubation pH ranges of 4.15-4.7 and 10.2-10.5 in increments of 0.05 pH units. Myosin heavy chain analysis (as well as a regression analysis comparing fiber type area and relative myosin heavy chain content) verified the mATPase-based fiber types. The pH ranges of mATPase stability/lability for the control samples were as previously reported, and support the use of preincubation pH values of 4.3, 4.6, and 10.4 for the delineation of fiber types in normal human muscle. For the postmortem samples, both quantitative and qualitative changes altered the pH ranges of mATPase activation/inactivation. Quantitative changes consisted of a time-dependent loss of mATPase activity that was inhibited in all fibers outside the pH range of 4.15-10.50. In addition, qualitative changes caused "shifts to the left" in mATPase stability within the fast fiber types (IIA and IIB). As such, complete inhibition of mATPase activity did not occur until preincubation at pH 4.45 and pH 4.30 for fiber types IIA and IIB, respectively. For the postmortem vastus lateralis muscle samples, optimal preincubation pH values for mATPase-based fiber type delineation were pH 4.30, 4.45, and 10.35. The reason for these qualitative changes in mATPase stability is not known. However, postmortem changes such as increased lactate production and marked acidification may play a role.     

Aging affects different human muscles in various ways. An image analysis of the histomorphometric characteristics of fiber types in human masseter and vastus lateralis muscles from young adults and the very old

This study is an attempt to objectively evaluate age-related changes in human muscles by use of histomorphometric methods. Aging in humans induces dramatic transformations in the skeletal muscles but little is known as to whether or not the aging processes per se may affect all muscles equally. In this study aging of two human muscles with different functions, origin and nerve supply is compared. Sections were cut from masseter and vastus lateralis muscles obtained from young adults aged 18-24 years and from the very old aged 90-102 years. Muscle fiber types were classified with the traditional myofibrillar ATPase staining. Various histomorphometric parameters of the different fiber types in human masseter and vastus lateralis muscle sections were obtained by image analyses to evaluate the age-related changes in the muscle fibers. The following variables were calculated: the number of each fiber type per photographed area; the area of each fiber and two indicators for the shape of the muscle fibers. In the aging muscles there was no relative preferential loss of a fiber type. High numbers of intermediate ATPase-stained fibers (IM fibers) were found in some old vastus muscles but were only sporadic in young vastus muscles. However, there was no change in the percentage distribution of intermediate ATPase-stained fibers when young and very old human masseter muscles were compared. Incubation of the sections with antimyosin antibodies showed that the IM fibers in old masseter and old vastus contained different myosin heavy chains. Thus ATPase activity and anti-myosin staining displayed a somewhat different pattern of fiber type distribution. The main changes in the shape and area indicated that type I fibers in the masseter became more circular while in the vastus they decreased significantly in size. The type II fibers in the vastus became very small and deviated significantly from circularity whereas the type II fibers in the masseter only exhibited a decrease in the size of the fibers. Histomorphometric measurements show that aging affects different human muscles in various ways.     

Fiber type and myosin heavy chain compositions of adult pretarsal orbicularis oculi muscle

Summary Pretarsal orbicularis oculi muscle (POOM) is an important structure of eyelid movement in human. The aim of this study was to investigate fiber histomorphology and myosin heavy chain (MyHC) isoform composition of adult POOM, and to clarify their age-related changes. Eyelid specimens from 58 subjects (age range, 21 to 91 years) were collected during upper blepharoplasty procedures. Serial cross sections of POOM were ATPase-stained and examined under miscroscope. Quantitative measures of muscle fiber size and fiber type distribution were obtained in 35 subjects with adequate fiber cross sections. Relative MyHC isoform contents of POOM were retrieved by gel electrophoresis in all 58 subjects. Examination of the histochemical staining revealed an abundance of type II fiber ( >85%) in human POOM, with more type IIX than IIA fibers. Decreased mean area of all fibers and type IIA fibers were noted in the old group when compared to the young. As for MyHC analysis, the relative content of MyHC isoforms exhibited an order of IIX > IIA > I, and the relative MyHC IIA content showed a negative correlation with age. Comparing with previous studies of limb or masticatory muscles, adult POOM exhibits a unique fiber and MyHC composition, as well as a different aging pattern.     

Muscle hypertrophy and fast fiber type conversions in heavy resistance-trained women

Twenty-four women completed a 20-week heavy-resistance weight training program for the lower extremity. Workouts were twice a week and consisted of warm-up exercises followed by three sets each of full squats, vertical leg presses, leg extensions, and leg curls. All exercises were performed to failure using 6-8 RM (repetition maximum). Weight training caused a significant increase in maximal isotonic strength (1 RM) for each exercise. After training, there was a decrease in body fat percentage (p less than 0.05), and an increase in lean body mass (p less than 0.05) with no overall change in thigh girth. Biopsies were obtained before and after training from the superficial portion of the vastus lateralis muscle. Sections were prepared for histological and histochemical examination. Six fiber types (I, IC, IIC, IIA, IIAB, and IIB) were distinguished following routine myofibrillar adenosine triphosphatase histochemistry. Areas were determined for fiber types I, IIA, and IIAB + IIB. The heavy-resistance training resulted in significant hypertrophy of all three groups: I (15%), IIA (45%), and IIAB + IIB (57%). These data are similar to those in men and suggest considerable hypertrophy of all major fiber types is also possible in women if exercise intensity and duration are sufficient. In addition, the training resulted in a significant decrease in the percentage of IIB with a concomitant increase in IIA fibers, suggesting that strength training may lead to fiber conversions.     

The KATP channel Kir6.2 subunit content is higher in glycolytic than oxidative skeletal muscle fibers

It has long been suggested that in skeletal muscle, the ATP-sensitive K(+) channel (K(ATP)) channel is important in protecting energy levels and that abolishing its activity causes fiber damage and severely impairs function. The responses to a lack of K(ATP) channel activity vary between muscles and fibers, with the severity of the impairment being the highest in the most glycolytic muscle fibers. Furthermore, glycolytic muscle fibers are also expected to face metabolic stress more often than oxidative ones. The objective of this study was to determine whether the t-tubular K(ATP) channel content differs between muscles and fiber types. K(ATP) channel content was estimated using a semiquantitative immunofluorescence approach by staining cross sections from soleus, extensor digitorum longus (EDL), and flexor digitorum brevis (FDB) muscles with anti-Kir6.2 antibody. Fiber types were determined using serial cross sections stained with specific antimyosin I, IIA, IIB, and IIX antibodies. Changes in Kir6.2 content were compared with changes in CaV1.1 content, as this Ca(2+) channel is responsible for triggering Ca(2+) release from sarcoplasmic reticulum. The Kir6.2 content was the lowest in the oxidative soleus and the highest in the glycolytic EDL and FDB. At the individual fiber level, the Kir6.2 content within a muscle was in the order of type IIB > IIX > IIA ≥ I. Interestingly, the Kir6.2 content for a given fiber type was significantly different between soleus, EDL, and FDB, and highest in FDB. Correlations of relative fluorescence intensities from the Kir6.2 and CaV1.1 antibodies were significant for all three muscles. However, the variability in content between the three muscles or individual fibers was much greater for Kir6.2 than for CaV1.1. It is suggested that the t-tubular K(ATP) channel content increases as the glycolytic capacity increases and as the oxidative capacity decreases and that the expression of K(ATP) channels may be linked to how often muscles/fibers face metabolic stress.     

Skeletal muscle histology and biochemistry of an elite sprinter, the African cheetah

To establish a skeletal muscle profile for elite sprinters, we obtained muscle biopsy samples from the vastus lateralis, gastrocnemius and soleus of African cheetahs (Acinonyx jubatus). Muscle ultrastructure was characterized by the fiber type composition and mitochondrial volume density of each sample. Maximum enzyme activity, myoglobin content and mixed fiber metabolite content were used to assess the major biochemical pathways. The results demonstrate a preponderance of fast-twitch fibers in the locomotor muscles of cheetahs; 83% of the total number of fibers examined in the vastus lateralis and nearly 61% of the gastrocnemius were comprised of fast-twitch fibers. The total mitochondrial volume density of the limb muscles ranged from 2.0 to 3.9% for two wild cheetahs. Enzyme activities reflected the sprinting capability of the cheetah. Maximum activities for pyruvate kinase and lactate dehydrogenase in the vastus lateralis were 1519.00 ± 203.60 and 1929.25±482.35 μmol min⁻¹ · g wet wt⁻¹, respectively, and indicated a high capacity for glycolysis. This study demonstrates that the locomotor muscles of cheetahs are poised for anaerobically based exercise. Fiber type composition, mitochondrial content and glycolytic enzyme capacities in the locomotor muscles of these sprinting cats are at the extreme range of values for other sprinters bred or trained for this activity including greyhounds, thoroughbred horses and elite human athletes. Accepted: 5 June 1997     

Muscle fiber characteristics of competitive power lifters

To examine the skeletal muscle characteristics of power lifters, 5 competitive power lifters (PL; X +/- SE; age = 31.0 +/- 1.5 years, squat = 287.7 +/- 15.7 kg, bench press = 170.5 +/- 17.7 kg, and deadlift = 284.2 +/- 7.5 kg) and 5 untrained control subjects (CON; age = 27.3 +/- 3.3 years) served as subjects. Isokinetic squat force and power was greater (p < 0.05) for the PL at all bar velocities (0.20, 0.82, and 1.43 m;pd s(-1)), as was vertical jump height and estimated power. Muscle biopsies from the vastus lateralis m. revealed significant differences for percent fiber type (PL, IIA = 45.5 +/- 1.6%, IIB = 1.3 +/- 0.8%; CON, IIA = 33.4 +/- 3.1%, IIB = 12.0 +/- 2.4%); percent fiber type area (PL, IIA = 51.8 +/- 1.6%, IIB = 1.3 +/- 0.8%; CON, IIA = 43.5 +/- 3.4%, IIB = 12.4 +/- 2.6%); and percent myosin heavy chain isoform (PL, IIa = 59.5 +/- 6.1%; CON, 46.5 +/- 2.5%). Muscle fiber characteristics were significantly correlated (r = +/- 0.61) with numerous strength and power measures for the PL. These data illustrate the muscle fiber characteristics necessary for the maximal force production requirements of power lifting.     

Expression of Myosin heavy chain isoforms in rat soleus muscle spindles after 19 days of hypergravity.

The aim of this study was to determine whether a period of 19 days in hypergravity was long enough to induce changes in the expression of myosin heavy chain (MyHC) isoforms in the muscle spindles. The soleus muscle of 10 male Wistar rats (control: CONT, n=5; hypergravity: HG, n=5) was frozen, cut into serial sections, and labeled with antibodies against MyHCs: I, IIA, IIA + IIX + IIB, slow-tonic, and alpha-cardiac. Forty CONT and 45 HG spindles were analyzed. The results from HG spindles compared to CONT showed that there was no change in the cross-sectional area of intrafusal fibers. However, along the entire length of B1 fibers, the expression of both MyHC I and alpha-cardiac was increased significantly, whereas the labeling against MyHC IIA and MyHC slow-tonic was decreased. In B2 fibers, the labeling against MyHC IIA (region A), slow-tonic (region A), and fast myosins (regions A-C) was statistically decreased. In chain fibers, the labeling against both MyHC IIA and fast MyHC was reduced significantly. We conclude that hypergravity has a real impact on the MyHC content in the muscle spindles and induces some inverse changes of those observed in hypogravity for MyHCs I, alpha-cardiac, and slow-tonic.